ID CYSI_XANAC Reviewed; 568 AA. AC Q8PHC8; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 15-FEB-2017, entry version 86. DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component {ECO:0000255|HAMAP-Rule:MF_01540}; DE Short=SiR-HP {ECO:0000255|HAMAP-Rule:MF_01540}; DE Short=SiRHP {ECO:0000255|HAMAP-Rule:MF_01540}; DE EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01540}; GN Name=cysI {ECO:0000255|HAMAP-Rule:MF_01540}; GN OrderedLocusNames=XAC3331; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- FUNCTION: Component of the sulfite reductase complex that CC catalyzes the 6-electron reduction of sulfite to sulfide. This is CC one of several activities required for the biosynthesis of L- CC cysteine from sulfate. {ECO:0000255|HAMAP-Rule:MF_01540}. CC -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 CC NADPH. {ECO:0000255|HAMAP-Rule:MF_01540}. CC -!- COFACTOR: CC Name=siroheme; Xref=ChEBI:CHEBI:60052; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540}; CC Note=Binds 1 siroheme per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01540}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01540}; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; CC hydrogen sulfide from sulfite (NADPH route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01540}. CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, CC the beta component is a hemoprotein. {ECO:0000255|HAMAP- CC Rule:MF_01540}. CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S CC domain family. {ECO:0000255|HAMAP-Rule:MF_01540}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE008923; AAM38174.1; -; Genomic_DNA. DR RefSeq; WP_011052200.1; NC_003919.1. DR ProteinModelPortal; Q8PHC8; -. DR STRING; 190486.XAC3331; -. DR EnsemblBacteria; AAM38174; AAM38174; XAC3331. DR KEGG; xac:XAC3331; -. DR PATRIC; 24058797; VBIXanAxo33670_3450. DR eggNOG; ENOG4105ET1; Bacteria. DR eggNOG; COG0155; LUCA. DR HOGENOM; HOG000218418; -. DR KO; K00381; -. DR OMA; GKYNMYL; -. DR OrthoDB; POG090I01HZ; -. DR UniPathway; UPA00140; UER00207. DR Proteomes; UP000000576; Chromosome. DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.480.10; -; 2. DR HAMAP; MF_01540; CysI; 1. DR InterPro; IPR011786; CysI. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom. DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS. DR Pfam; PF01077; NIR_SIR; 2. DR Pfam; PF03460; NIR_SIR_ferr; 2. DR PRINTS; PR00397; SIROHAEM. DR SUPFAM; SSF55124; SSF55124; 2. DR TIGRFAMs; TIGR02041; CysI; 1. DR PROSITE; PS00365; NIR_SIR; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; Complete proteome; KW Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP; KW Oxidoreductase. FT CHAIN 1 568 Sulfite reductase [NADPH] hemoprotein FT beta-component. FT /FTId=PRO_0000388527. FT METAL 425 425 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. FT METAL 431 431 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. FT METAL 470 470 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. FT METAL 474 474 Iron (siroheme axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01540}. FT METAL 474 474 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. SQ SEQUENCE 568 AA; 62418 MW; 4E86EDBFF11AE961 CRC64; MSHSVEDIKS ESRRLRGSLE QSLADAVTGA LREDDQTLIK YHGSYQQDDR DIRDERRRQK LEPAYQFMIR TRTPGGVITP TQWLALDGIA TRYANHSLRI TTRQAFQFHG VIKRELKATM QAINATLIDT LAACGDVNRN VQVAANPLLS QAHATLYADA ARVSEHLLPN TRAYYEIWLD EERVSGSGSE DEPIYGERYL PRKFKIGFAA PPLNDVDVFA NDLGFIAILR DGQLLGYNVS IGGGMGASHG DAETWPRVAN VIGFVTREQL LDIATAVVTT QRDFGNRAVR KRARFKYTID DHGLDTIVAE IARRAGFALQ PAQPFAFDHN GDRYGWVEGE DGLWHLTLSL PAGRIADTDT AAHLSGLRAI AQLNVGEFRM TPNQNLVIAG VLASERARVD ALVAHYGLDA GNQSATALAR GAMACVALPT CGLAMAEAER YLPDFGAALQ PLLQQHGLAE TPIVLRLSGC PNGCSRPYLA EIALVGKAPG RYNLMLGGDR RGQRLNTLYR ENITEPEILA ALEPLLARYA AERDHANDEG FGDFLHRAGV IALPPYPTHR RLDLELLA //